ID   CP142_MYCTO             Reviewed;         372 AA.
AC   P9WPL4; D0EW73; F2GEM8; O53563;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Steroid C26-monooxygenase {ECO:0000250|UniProtKB:P9WPL5};
DE            EC=1.14.15.28 {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Cholest-4-en-3-one C26-monooxygenase {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Cholesterol C26-monooxygenase {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Cytochrome P450 142 {ECO:0000250|UniProtKB:P9WPL5};
DE   AltName: Full=Steroid C27-monooxygenase {ECO:0000250|UniProtKB:P9WPL5};
GN   Name=cyp142; OrderedLocusNames=MT3619;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the utilization of cholesterol as the sole carbon
CC       and energy source by degrading the side chain during infection.
CC       Primarily catalyzes the sequential oxidation of the terminal methyl of
CC       cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol),
CC       (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the
CC       carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to
CC       sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
CC       {ECO:0000250|UniProtKB:P9WPL5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
CC         [ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized
CC         [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:71570; EC=1.14.15.28;
CC         Evidence={ECO:0000250|UniProtKB:P9WPL5};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P9WPL5};
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000250|UniProtKB:P9WPL5}.
CC   -!- INDUCTION: By cholesterol. {ECO:0000250|UniProtKB:P9WPL5}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47979.1; -; Genomic_DNA.
DR   PIR; H70807; H70807.
DR   RefSeq; WP_003917809.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPL4; -.
DR   SMR; P9WPL4; -.
DR   BindingDB; P9WPL4; -.
DR   EnsemblBacteria; AAK47979; AAK47979; MT3619.
DR   KEGG; mtc:MT3619; -.
DR   PATRIC; fig|83331.31.peg.3898; -.
DR   HOGENOM; CLU_033716_0_2_11; -.
DR   UniPathway; UPA01058; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0031073; F:cholesterol 26-hydroxylase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; Heme; Iron; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase; Steroid metabolism;
KW   Sterol metabolism; Virulence.
FT   CHAIN           1..372
FT                   /note="Steroid C26-monooxygenase"
FT                   /id="PRO_0000426931"
FT   BINDING         314
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPL5"
SQ   SEQUENCE   372 AA;  41440 MW;  B9A858B8D7D1D3A0 CRC64;
     MRANQPVFRD RNGLAAASTY QAVIDAERQP ELFSNAGGIR PDQPALPMMI DMDDPAHLLR
     RKLVNAGFTR KRVKDKEASI AALCDTLIDA VCERGECDFV RDLAAPLPMA VIGDMLGVRP
     EQRDMFLRWS DDLVTFLSSH VSQEDFQITM DAFAAYNDFT RATIAARRAD PTDDLVSVLV
     SSEVDGERLS DDELVMETLL ILIGGDETTR HTLSGGTEQL LRNRDQWDLL QRDPSLLPGA
     IEEMLRWTAP VKNMCRVLTA DTEFHGTALC AGEKMMLLFE SANFDEAVFC EPEKFDVQRN
     PNSHLAFGFG THFCLGNQLA RLELSLMTER VLRRLPDLRL VADDSVLPLR PANFVSGLES
     MPVVFTPSPP LG